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The structure of VgrG1, the needle tip of the bacterial Type VI Secretion SystemThe structure of VgrG1, the needle tip of the bacterial Type VI Secretion System
Structural highlights
FunctionVGR1A_PSEAE Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:21325275, PubMed:24794869). Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1/Hcp1 (PubMed:26894531). Allows the delivery of the Tse6 toxin to target cells where it exerts its toxicity (PubMed:30177742).[1] [2] [3] [4] Publication Abstract from PubMedWhen 300 kV cryo-EM images at Scherzer focus are acquired from approximately 100 nm thick three-dimensional protein nanocrystals using a Falcon 2 direct electron detector, Fourier transformation can reveal the crystalline lattice to surprisingly high resolutions, even though the images themselves seem to be devoid of any contrast. Here, it is reported how this lattice information can be enhanced by means of a wave finder in combination with Wiener-type maximum-likelihood filtering. This procedure paves the way towards full three-dimensional structure determination at high resolution for protein crystals. Lattice filter for processing image data of three-dimensional protein nanocrystals.,van Genderen E, Li YW, Nederlof I, Abrahams JP Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):34-9. doi:, 10.1107/S205979831502149X. Epub 2016 Jan 1. PMID:26894532[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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